Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q96V34 (LPSA1_EPIFI)

Entry version 85 (18 Sep 2019)
Sequence version 2 (07 Feb 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

D-lysergyl-peptide-synthetase subunit 1

Gene

lpsA

Organism
Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

D-lysergyl-peptide-synthetase subunit 1; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD+, resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ergot alkaloid biosynthesis

This protein is involved in the pathway ergot alkaloid biosynthesis, which is part of Alkaloid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ergot alkaloid biosynthesis and in Alkaloid biosynthesis.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase, Transferase

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00327

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
D-lysergyl-peptide-synthetase subunit 11 Publication (EC:2.3.1.-1 Publication)
Short name:
LPSA1 Publication
Alternative name(s):
Ergot alkaloid synthesis protein lpsA1 Publication
Nonribosomal peptide synthetase lpsA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:lpsA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEpichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri73839 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Clavicipitaceae › Epichloe ›

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes the production of ergovaline (PubMed:11592979).1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004391071 – 3589D-lysergyl-peptide-synthetase subunit 1Add BLAST3589

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei915O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2006O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei3096O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q96V34

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini883 – 952Carrier 1PROSITE-ProRule annotationAdd BLAST70
Domaini1974 – 2042Carrier 2PROSITE-ProRule annotationAdd BLAST69
Domaini3064 – 3132Carrier 3PROSITE-ProRule annotationAdd BLAST69

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni344 – 742Adenylation (A) domain 1Sequence analysisAdd BLAST399
Regioni995 – 1380Condensation (C) domain 1Sequence analysisAdd BLAST386
Regioni1424 – 1826Adenylation (A) domain 2Sequence analysisAdd BLAST403
Regioni2087 – 2509Condensation (C) domain 2Sequence analysisAdd BLAST423
Regioni2534 – 2929Adenylation (A) domain 3Sequence analysisAdd BLAST396
Regioni3187 – 3585Cyclization (Cyc) domainSequence analysisAdd BLAST399

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) or reductase domain (R) that releases the newly synthesized peptide from the enzyme (By similarity). LpsA1 has a domain arrangement (A-T-C-A-T-C-A-T-Cyc) with 3 A and 3 peptidyl carrier (PCP/T) domains, 2 C-domains, and a terminal domain called the Cyc domain (By similarity). The Cyc domain has limited similarity to both C and Cy domains of NRPS but is most different in the so-called C3 and Cy3 motif of the latter domains, suggesting a special mechanism in acyl diketopiperazine formation, which is the final step of D-lysergyl peptide lactam synthesis (By similarity). LpsA misses an N-terminal C domain in the first module, leading to the conclusion that this C domain is located on the other subunit (lpsB) containing the D-lysergic acid module (By similarity).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NRP synthase family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 4 hits
PF00550 PP-binding, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00823 PKS_PP, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336 SSF47336, 3 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01733 AA-adenyl-dom, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q96V34-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSTTVEPVG STYARPKPLG NLDHRIEQLL GSESVLNESP GHSPNAYGIP 
        60         70         80         90        100
YTARNLTLED VDHCKSLTNK DLSLEFWKSH LQTAKPCILT RLKPGTGSSI 
       110        120        130        140        150
LSSRQSVKVD LGGVNTTCRN LFDSTGISLM TVFKVAWGMV LSTYTGSDHV 
       160        170        180        190        200
CFGYGAARPS MSVDGEQTTI KPLIKMLPCD MLFKGGTTLL GTVHKAESDF 
       210        220        230        240        250
ICTIPYQSVS IAEIHHGIGT ESGALFNTSI IFWPQEDFSD NPITEVLSQK 
       260        270        280        290        300
VTETESLTEC DIIMHVDSKQ QCYLSYWDYF LSDEQANHLA GALNVAMKSI 
       310        320        330        340        350
FESPHRPVGQ VEMFSYLDQQ KLLQWNGQAP IASESCLGDL IGQNCHSRPD 
       360        370        380        390        400
SLAVDSWDGF FTYQELDRLS STLANKLRCA GVGPDVFVTA CFDRCKWMPV 
       410        420        430        440        450
AMLGIIKAGG AICALDPSYP LGRLTGMCQL LKSTVVLTTA NNAQQAEQLA 
       460        470        480        490        500
LTTIVLGNDL WTGDSYDEQE RQAPLSNVCP SNALYAVFTS GSTGKPKGVV 
       510        520        530        540        550
VEHRSFSSCA LASLKPLDIR PHDRVLHISS YAFDISIFET LATLTAGASV 
       560        570        580        590        600
AIPSEKARRE DLPGAMRELQ ATWAFLTPTV ARMYQPKDFP SLRTLCLGGE 
       610        620        630        640        650
AIHTSDIGLW ASKNLVTGYN PAESCPLGIS GPADKSAASF LGWSFSSQAS 
       660        670        680        690        700
WIVDPRDYQK LAPIGAVGEL MIEGPAVARG YIHDLTCSHP DSPFVLPPPQ 
       710        720        730        740        750
WLSRFRASTS QDTRLYRTGD LVQYGSNGSV HFIGRKDLQV KVHGQRVELS 
       760        770        780        790        800
EIEFQLHKTL LPLDCKVVVD AVTFTGHTSV IAFITAAEHS DLENEDDAVR 
       810        820        830        840        850
SPDVKVITQD FEIRAADAAT KLQSILPRHM VPTIYLPVGH IPMSRSGKID 
       860        870        880        890        900
RQKLRSLALS LPRETLYHIG RQPGPGEIVV TDVERRLQLL FAQVLDLSPE 
       910        920        930        940        950
KIKADSDFFR LGGDSIYAMK LLALAPQQGP RDLTYEEIFR HPKLRDLAAA 
       960        970        980        990       1000
SSSFSNISLA IPEDLGPAPF SLARDADSLT KIASEQCGVA VGDIEDIYPC 
      1010       1020       1030       1040       1050
TSLQESLIAS TAHDQDAYVG VQSFTLNDDI DTTRLKMAWK MTSEGHPILR 
      1060       1070       1080       1090       1100
TRIIQTDSGA PYQAVIRGPL SWSEESSSDD LPPQFQPSIG LGTPLVQLCL 
      1110       1120       1130       1140       1150
TNSRLLVAMH HALYDGWSLP LLLAEVDQAY RQLSVRQLPP FNRYVKHVTE 
      1160       1170       1180       1190       1200
TVDSAASFWK AELQDADPVD FPPLPHLNYK PEPRALLTKS ITLTAHTNSQ 
      1210       1220       1230       1240       1250
HNVTLATELQ LAWALTSHTY TNSQDVVFGI ISSGRGAPVA GIERMLGPTF 
      1260       1270       1280       1290       1300
ASTPLRVPLD PAQDVREALE ELQYRLAEQT KYVQIGLQRI RQQGPNAAAA 
      1310       1320       1330       1340       1350
CSFQTMLVVE PNQPVKTQSA WFSRHEFLSE LTRFSSHSLT LRCKLLAGSV 
      1360       1370       1380       1390       1400
EVTAIYDQLV VPDAQMQRIL SQFQHILTQI QGIGSRDTTI GDIDRLSSGD 
      1410       1420       1430       1440       1450
WNELQAWNST LPPGLELSVH QMVQAKAQMQ PEALAIHSWD GDLTYKELED 
      1460       1470       1480       1490       1500
YAKGLANRLH ALGVRPNTFV AIYLQKSLWV VVAQLAVLIA GAAFTTLETS 
      1510       1520       1530       1540       1550
QPINRLRDVC RTVQPTVVLT SDKLRLSGAD LEVPAPLLVI NQQLLLEEPG 
      1560       1570       1580       1590       1600
SHSRPLENHT IMASDAMYSI ATSGTTGKPK VVVIEHQAFL ANSKHLIDRW 
      1610       1620       1630       1640       1650
GFTADSRVLQ FAGYSFDAMI VEHFITLLAG GCICIPSSFD RDNRLATCIV 
      1660       1670       1680       1690       1700
EMRVNWAMLT SSVIPLFTPA AVPTLQTLVQ AGEPMHQGIT DCWASHVQLF 
      1710       1720       1730       1740       1750
NAYGPTECSV ISTTSNIINP DARNPRNIGF TTGGVCWIVD PENPESPPVP 
      1760       1770       1780       1790       1800
IGAEGELIIE GAILARGYLG DRVRTAAAFT LRPGWLDDFR GSSGDNRIYR 
      1810       1820       1830       1840       1850
TGDIVRYDPD GSISYVRRKD SQVKLRGQRV ELLDVEHHLQ NCFPGALQVV 
      1860       1870       1880       1890       1900
ADIVTVPNTQ SSALVALVLA TPTSSSSVAI ESCSNDDQAT TAHGLLLLAN 
      1910       1920       1930       1940       1950
NPQFLIDASA AELALQDRVP SYMVPSLFIP TSRFPRDVSG KVNRGEITRS 
      1960       1970       1980       1990       2000
LAALSRQEWD GYVSTNRVAP TSGLERELQK IWARILNIPP DTIGVHDSFF 
      2010       2020       2030       2040       2050
RLGGDSITCM QVAAQCSRTG ILITVKDIFK RRTIEKLAAA AVVVQCPESS 
      2060       2070       2080       2090       2100
TTERVNTAEA KFSFYGPGQL EEYMIQIQPQ LGEGQVVEDI YPCSPIQRGI 
      2110       2120       2130       2140       2150
LMSHARNSGN YEEVIQWKVI SRAPVDVCRL RDAWAQVVDR HAVLRTLFLH 
      2160       2170       2180       2190       2200
VCKENYLDQV VLRSHSPMVL VYNEGEEPVN PVSTGCSQPM HHLRVKRSSA 
      2210       2220       2230       2240       2250
GGITVRLHIN HALVDGASLF IIRRDLAMAY EGRLASSRAS SPYRDYIAYL 
      2260       2270       2280       2290       2300
QNCHSQIQSN EYWQSYMEGT APCLFPTLKN AGAQDSQQPF EAFTLQLGAT 
      2310       2320       2330       2340       2350
ADLNQFCENH RLALTSVLHV VWAMVVQRYT AMDEVCFGYM TSGRHVPVAG 
      2360       2370       2380       2390       2400
VQDIVGPLFN MLVARVGLPH DATLLSVMQK YHDNFLISLD HQHQSLAETL 
      2410       2420       2430       2440       2450
HSIGSASGEL FNTLVSIFND QREGEPAHKS SAVTLVGDDI HSRSEYAITL 
      2460       2470       2480       2490       2500
NVLMLADQVH IQLSYHTSWL SDNYARMIAE TFRHVLATVL GQPQLRLNEI 
      2510       2520       2530       2540       2550
EMLDEEHRSG LYGRNHAAVP SFDSCIHYTI HQRCLESPES PAICAWDGDF 
      2560       2570       2580       2590       2600
SYRRLDQLSS SLAEELIGHG VGVEMTIPVL LEKTCWTPVA MLAVLKSGAS 
      2610       2620       2630       2640       2650
FVLMDASHPL GRLQTICEAI NPPVILASPQ TRSKAVGLTS HVIEVTNRLL 
      2660       2670       2680       2690       2700
EQEQAEQQQT WPRVVTKGSN AAYVVFTSGS TGKPKGAIVD HSCLATAAGH 
      2710       2720       2730       2740       2750
LPSRMYINSA SRVLQFSSHA WDIPVTDVLL TLRVGGCVCI PSDEERIGNL 
      2760       2770       2780       2790       2800
AQVANRMMVN WALLTPTVAR LVKPEDFTHL QTLVLAGEAV SSTDLTTWHD 
      2810       2820       2830       2840       2850
KVRLIQGYGP AECSLVSTVS EPLTPSDNPR NIGQPNGCVA WVVHRDNHHL 
      2860       2870       2880       2890       2900
LAPSGAIEEL VLEGPIVSRG YINDPERSAA VFVDPPTWLT RLRGGHSPTR 
      2910       2920       2930       2940       2950
LYKTGDLVSA GLDGCLSFVG RKDDQVKIRG QRVELGEVEA LASQAFPGSH 
      2960       2970       2980       2990       3000
VVVETVKDLS STILVAFILQ KETAHAQPSS ISSLLHPPSP LFRELISAAS 
      3010       3020       3030       3040       3050
CSLRETMPSF MIPTVFLPLA HLPKAPTGKT DRKFLRGHVA SLSRMELEAY 
      3060       3070       3080       3090       3100
SIVDATGRAP STPLETRLQE LVGRVLHRSP ESIPLDEDLF TFGLDSLTAM 
      3110       3120       3130       3140       3150
TLATLVREDG LAISVPTIFQ RPRLSELAVV LNQEQQIKQG QFLAPPPNAL 
      3160       3170       3180       3190       3200
MASMDELCAQ WQLDRSQVVN IAPTTYYQRG SLASHHTNFI ALHFSQPLDP 
      3210       3220       3230       3240       3250
IPFRNAVVGL VQKHAILRTA FVPFRETFVQ LILRDFDLPV QEIRTDEDDP 
      3260       3270       3280       3290       3300
SVVAESFCRE ADRVPVSFGT PITQLYMILG RAGDRLSAVL RLQRAQYDGV 
      3310       3320       3330       3340       3350
AVSCMIADLR SAFDEAPSSA LPTLEYADYV ISRRAHSSPP VFQVWRELLQ 
      3360       3370       3380       3390       3400
GSSMTYLVPP TEYIRSTDRS RTELLVTSSC DIPMPDTKGG ITMATVIKTA 
      3410       3420       3430       3440       3450
WALCLARQTQ SKDVVFAQLV RNRHLAIAGI DRTVGPCINY VPVRASLNLD 
      3460       3470       3480       3490       3500
WTAKEFLHWV QRQHIRTMTC DMADWDDLVI ESTSWPRDTE LGSAVHYLSA 
      3510       3520       3530       3540       3550
PVASDYTFAG DVPCQFQMYD FKMVHTYPMV TCLPFPSVGD SSLTVLKIIL 
      3560       3570       3580 
TSAVFGQGVA DRLLSLFRDM VHRLTTYPES LVSELLIIR
Length:3,589
Mass (Da):394,889
Last modified:February 7, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8B8051761A23841B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF368420 Genomic DNA Translation: AAL26315.2

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368420 Genomic DNA Translation: AAL26315.2

3D structure databases

SMRiQ96V34
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00327

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
PfamiView protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 4 hits
PF00550 PP-binding, 3 hits
SMARTiView protein in SMART
SM00823 PKS_PP, 3 hits
SUPFAMiSSF47336 SSF47336, 3 hits
TIGRFAMsiTIGR01733 AA-adenyl-dom, 2 hits
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLPSA1_EPIFI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96V34
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2017
Last sequence update: February 7, 2006
Last modified: September 18, 2019
This is version 85 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again